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Database: UniProt
Entry: D8RVU4_SELML
LinkDB: D8RVU4_SELML
Original site: D8RVU4_SELML 
ID   D8RVU4_SELML            Unreviewed;       629 AA.
AC   D8RVU4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   ORFNames=SELMODRAFT_102593 {ECO:0000313|EMBL:EFJ24019.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ24019.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A.,
RA   Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L.,
RA   Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M.,
RA   DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L.,
RA   Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L.,
RA   Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y.,
RA   Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U.,
RA   Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E.,
RA   Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S.,
RA   Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M.,
RA   Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P.,
RA   Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L.,
RA   Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R.,
RA   Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S.,
RA   Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000256|RuleBase:RU363003};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000256|RuleBase:RU363003}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU363003}.
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DR   EMBL; GL377591; EFJ24019.1; -; Genomic_DNA.
DR   RefSeq; XP_002975234.1; XM_002975188.1.
DR   STRING; 88036.EFJ24019; -.
DR   EnsemblPlants; EFJ24019; EFJ24019; SELMODRAFT_102593.
DR   GeneID; 9629094; -.
DR   Gramene; EFJ24019; EFJ24019; SELMODRAFT_102593.
DR   KEGG; smo:SELMODRAFT_102593; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   InParanoid; D8RVU4; -.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; 911009at2759; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006236; PGDH.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001514};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN      557    629       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   629 AA;  65764 MW;  D5AAC9350596525F CRC64;
     MGAPAQISSA RAARGIAILE LPRSLLAGAR AARISSGAVA RKLGLVATRH ILGGSLHRGL
     AAKPPCAIAV EGSDISVRSQ AIEVISKPTV LVAEKLGEAG LELLRKVANV DCSYNLSPED
     LCAKISLCDA VIVRSGTKIT REVFEASNGR LKVVGRAGVG IDNVDLQAAT EMGCLVVNAP
     TANTVAAAEH GIALLAALAR NVAQANASVK SGKWQRNKFT GVSLVDKTIA VLGFGKVGSE
     VARRAKGLGM HVIAHDPYAP ADRARAIGVE LVSFDEALAR ADFISLHMPL TPATNKIFND
     ETFAKVKKGV RIVNVARGGV IDENSLVRAL NSGIVAQAAL DVFTKEPPEK DDKLVQHENV
     IVTPHLGAST AEAQEGVALE IAEAVVGALQ GELAATAVNA PMVPSEVLTE LAPYITLAER
     LGKLAVQLVA GGGGVKDITI SYNSARAPDD LDTRLLRAMI VKGLVEPVSD THINLVNADY
     IAKQRGLRIS EERHPAEGTE AAPLESIEVR IANVESRFSS AMSDSGDVSL AGRIKDGVPH
     LSQVGSFSID VSLEGSVILC RQVDQPGMIG KVGGLLGDEN VNISFMSVGR TSPRQKAVMA
     IGVDDEPSKE VLQKIGSISA VEELVFLKL
//
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